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J Biol Chem, Vol. 273, Issue 10, 5455-5460, March 6, 1998
From the Departments of Medicine and Pathology and the Molecular
Biology Program, University of Colorado Health Sciences Center,
Denver, Colorado 80262
The B-isoform of human progesterone receptors
(PR) contains three activation functions (AF3, AF1, and AF2), two of
which (AF1 and AF2) are shared with the A-isoform. AF3 is in the
B-upstream segment (BUS), the far N-terminal 164 amino acids of
B-receptors; AF1 is in the 392-amino acid N-terminal region common to
both receptors; and AF2 is in the C-terminal hormone binding domain. B-receptors are usually stronger transactivators than A-receptors due
to transcriptional synergism between AF3 and one of the two downstream
AFs. We now show that the N terminus of PR common to both isoforms
contains an inhibitory function (IF) located in a 292-amino acid
segment lying upstream of AF1. IF represses the activity of A-receptors
but is not inhibitory in the context of B-receptors due to constraints
imparted by BUS. As a result, IF inhibits AF1 or AF2 but not AF3,
regardless of the position of IF relative to BUS. IF is functionally
independent and strongly represses transcription when it is fused
upstream of estrogen receptors. These data demonstrate the existence of
a novel, transferable inhibitory function, mapping to the PR N
terminus, which begins to assign specific roles to this large undefined
region.
An N-terminal Inhibitory Function, IF, Suppresses
Transcription by the A-isoform but Not the B-isoform of Human
Progesterone Receptors
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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